Crystallographic structure of ATP:protein-L-histidine N-phosphotransferase based on the PDB: 2c2a coordinates.
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EC no.
2.7.13.3
CAS no.
99283-67-7
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Histidine kinases (HK) are multifunctional, and in non-animal kingdoms, typically transmembrane, proteins of the transferase class of enzymes that play a role in signal transduction across the cellular membrane.[1] The vast majority of HKs are homodimers that exhibit autokinase, phosphotransfer, and phosphatase activity. HKs can act as cellular receptors for signaling molecules in a way analogous to tyrosine kinase receptors (RTK). Multifunctional receptor molecules such as HKs and RTKs typically have portions on the outside of the cell (extracellular domain) that bind to hormone- or growth factor-like molecules, portions that span the cell membrane (transmembrane domain), and portions within the cell (intracellular domain) that contain the enzymatic activity. In addition to kinase activity, the intracellular domains typically have regions that bind to a secondary effector molecule or complex of molecules that further propagate signal transduction within the cell. Distinct from other classes of protein kinases, HKs are usually parts of a two-component signal transduction mechanisms in which HK transfers a phosphate group from ATP to a histidine residue within the kinase, and then to an aspartate residue on the receiver domain of a response regulator protein (or sometimes on the kinase itself). More recently, the widespread existence of protein histidine phosphorylation distinct from that of two-component histidine kinases has been recognised in human cells.[2][3] In marked contrast to Ser, Thr and Tyr phosphorylation, the analysis of phosphorylated Histidine using standard biochemical and mass spectrometric approaches is much more challenging,[4][5] and special procedures and separation techniques are required for their preservation alongside classical Ser, Thr and Tyr phosphorylation on proteins isolated from human cells.[6]
In terms of enzymology, a histidine kinase (EC 2.7.13.3, EnvZ, histidine protein kinase, protein histidine kinase, protein kinase (histidine), HK1, HP165, Sln1p) is an enzyme that catalyzes the chemical reaction
ATP + protein L-histidine ADP + protein N-phospho-L-histidine.
Thus, the two substrates of this enzyme are ATP and protein L-histidine, whereas its two products are ADP and protein N-phospho-L-histidine.
This type of enzyme is involved in signal transduction pathways upstream of many cellular processes including various metabolic, virulence, and homeostatic pathways.
^Wolanin PW, Thomason PA, Stock JB (2002). "Histidine protein kinases: key signal transducers outside the animal kingdom". Genome Biology. 3 (10): reviews3013.1–3013.8. doi:10.1186/gb-2002-3-10-reviews3013. PMC 244915. PMID 12372152.
^Fuhs SR, Hunter T (2017). "pHisphorylation: the emergence of histidine phosphorylation as a reversible regulatory modification". Curr Opin Cell Biol. 45: 8–16. doi:10.1016/j.ceb.2016.12.010. PMC 5482761. PMID 28129587.
^Fuhs SR, Meisenhelder J, Aslanian A, Ma L, Zagorska A, Stankova M, Binnie A, Al-Obeidi F, Mauger J, Lemke G, Yates JR 3rd, Hunter T (2015). "Monoclonal 1- and 3-Phosphohistidine Antibodies: New Tools to Study Histidine Phosphorylation". Cell. 162 (1): 198–210. doi:10.1016/j.cell.2015.05.046. PMC 4491144. PMID 26140597.
^Gonzalez-Sanchez MB, Lanucara F, Hardman GE, Eyers CE (2014). "Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer". Int J Mass Spectrom. 367: 28–34. Bibcode:2014IJMSp.367...28G. doi:10.1016/j.ijms.2014.04.015. PMC 4375673. PMID 25844054.
^Gonzalez-Sanchez MB, Lanucara F, Helm M, Eyers CE (2013). "Attempting to rewrite History: challenges with the analysis of histidine-phosphorylated peptides". Biochem Soc Trans. 41 (4): 1089–1095. doi:10.1042/bst20130072. PMID 23863184.
^Hardman G, Perkins S, Ruan Z, Kannan N, Brownridge P, Byrne DP, Eyers PA, Jones AR, Eyers CE (13 October 2017). "Extensive non-canonical phosphorylation in human cells revealed using strong-anion exchange-mediated phosphoproteomics". bioRxiv 10.1101/202820.
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